Research workbench
Structure of the E. COLI chaperone papd in complex with the pilin domain of the papgii adhesin
Analyse Structure of the E. COLI chaperone papd in complex with the pilin domain of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WMP
- Type
- protein
- Length
- 338 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15319, Q47445
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 215 | — | P15319 |
| B | — | protein | 123 | — | Q47445 |
Compared structures
- 2WMP · Structure of the E. coli chaperone PapD in complex with the pilin domain of the PapGII… · the same entry in another collection · chain A against A, TM-score 1.00
- P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P15319
- Every structure of UniProt Q47445
- Elsewhere: RCSB PDB 2WMP · PDBe 2WMP · UniProt P15319 · UniProt Q47445
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